Molecular insights into FucR transcription factor to control the metabolism of <sub>L</sub>-fucose in Bifidobacterium longum subsp. infantis.

Yang, Xiaojun; Zhang, Jing; Zhu, Jing; Yang, Ruijin; Tong, Yanjun

Molecular insights into FucR transcription factor to control the metabolism of _L-fucose in Bifidobacterium longum subsp. infantis.

Yang, Xiaojun; Zhang, Jing; Zhu, Jing; Yang, Ruijin; Tong, Yanjun.

Afiliación

Yang X; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
Zhang J; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
Zhu J; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
Yang R; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
Tong Y; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China. Electronic address: tongyanjun@jiangnan.edu.cn.

Microbiol Res ; 283: 127709, 2024 Jun.

Article en En | MEDLINE | ID: mdl-38593579

ABSTRACT

ABSTRACT

Bifidobacterium longum subsp. infantis commonly colonizes the human gut and is capable of metabolizing L-fucose, which is abundant in the gut. Multiple studies have focused on the mechanisms of L-fucose utilization by B. longum subsp. infantis, but the regulatory pathways governing the expression of these catabolic processes are still unclear. In this study, we have conducted a structural and functional analysis of L-fucose metabolism transcription factor FucR derived from B. longum subsp. infantis Bi-26. Our results indicated that FucR is a L-fucose-sensitive repressor with more α-helices, fewer ß-sheets, and ß-turns. Transcriptional analysis revealed that FucR displays weak negative self-regulation, which is counteracted in the presence of L-fucose. Isothermal titration calorimetry indicated that FucR has a 21 stoichiometry with L-fucose. The key amino acid residues for FucR binding L-fucose are Asp280 and Arg331, with mutation of Asp280 to Ala resulting in a decrease in the affinity between FucR and L-fucose with the Kd value from 2.58 to 11.68â¯µM, and mutation of Arg331 to Ala abolishes the binding ability of FucR towards L-fucose. FucR specifically recognized and bound to a 20-bp incomplete palindrome sequence (5'-ACCCCAATTACGAAAATTTTT-3'), and the affinity of the L-fucose-loaded FucR for the DNA fragment was lower than apo-FucR. The results provided new insights into the regulating L-fucose metabolism by B. longum subsp. infantis.

Asunto(s)

Bifidobacterium longum; Bifidobacterium; Humanos; Bifidobacterium/genética; Bifidobacterium/metabolismo; Fucosa/metabolismo; Factores de Transcripción/genética; Factores de Transcripción/metabolismo; Metabolismo de los Hidratos de Carbono; Bifidobacterium longum/genética; Bifidobacterium longum/metabolismo

Palabras clave

(L-)fucose; Bifidobacterium longum subsp. infantis; Carbohydrate metabolism; Transcription factor

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bifidobacterium / Bifidobacterium longum Límite: Humans Idioma: En Revista: Microbiol Res Asunto de la revista: MICROBIOLOGIA / SAUDE AMBIENTAL Año: 2024 Tipo del documento: Article Pais de publicación: Alemania

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